Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes.

ABSTRACT: For many years seven transmembrane domain G protein-coupled receptors (GPCRs) were thought to exist and function exclusively as monomeric units. However, evidence both from native cells and heterologous expression systems has demonstrated that GPCRs can both traffic and signal within higher-order complexes. As for other protein-protein interactions, conformational changes in one polypeptide, including those resulting from binding of pharmacological ligands, have the capacity to alter the conformation and therefore the response of the interacting protein(s), a process known as allosterism. For GPCRs, allosterism across homo- or heteromers, whether dimers or higher-order oligomers, represents an additional topographical landscape that must now be considered pharmacologically. Such effects ma

SUBMITTER: Smith NJ 

PROVIDER: S-EPMC2993260 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature